2hr7

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spinqualitylabelsall models 2hr7, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Insulin receptor (domains 1-3)

Overview

The insulin receptor (IR) and the type-1 insulin-like growth factor, receptor (IGF1R) are homologous multidomain proteins that bind insulin and, IGF with differing specificity. Here we report the crystal structure of, the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and, compare it with the previously determined structure of the corresponding, fragment of IGF1R. The most important differences seen between the two, receptors are in the two regions governing ligand specificity. The first, is at the corner of the ligand-binding surface of the L1 domain, where the, side chain of F39 in IR forms part of the ligand binding surface involving, the second (central) beta-sheet. This is very different to the location of, its counterpart in IGF1R, S35, which is not involved in ligand binding., The second major difference is in the sixth module of the CR domain, where, IR contains a larger loop that protrudes further into the ligand-binding, pocket. This module, which governs IGF1-binding specificity, shows, negligible sequence identity, significantly more alpha-helix, an, additional disulfide bond, and opposite electrostatic potential compared, to that of the IGF1R.

About this Structure

2HR7 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity., Lou M, Garrett TP, McKern NM, Hoyne PA, Epa VC, Bentley JD, Lovrecz GO, Cosgrove LJ, Frenkel MJ, Ward CW, Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12429-34. Epub 2006 Aug 7. PMID:16894147

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